6mm1 - Revision history

OCA at 10:08, 22 May 2024

2024-05-22T10:08:34Z

←Older revision		Revision as of 10:08, 22 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6mm1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MM1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[6mm1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MM1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.9Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mm1 OCA], [https://pdbe.org/6mm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mm1 RCSB], [https://www.ebi.ac.uk/pdbsum/6mm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mm1 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mm1 OCA], [https://pdbe.org/6mm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mm1 RCSB], [https://www.ebi.ac.uk/pdbsum/6mm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mm1 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:05, 18 May 2023

2023-05-18T07:05:38Z

←Older revision		Revision as of 07:05, 18 May 2023
Line 3:		Line 3:
	<StructureSection load='6mm1' size='340' side='right'caption='[[6mm1]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='6mm1' size='340' side='right'caption='[[6mm1]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6mm1]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MM1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6MM1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6mm1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MM1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EHMT2, BAT8, C6orf30, G9A, KMT1C, NG36 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mm1 OCA], [https://pdbe.org/6mm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mm1 RCSB], [https://www.ebi.ac.uk/pdbsum/6mm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mm1 ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mm1 OCA], [~~http~~://pdbe.org/6mm1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6mm1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6mm1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6mm1 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/EHMT2_HUMAN EHMT2_HUMAN]] Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.<ref>PMID:8457211</ref> <ref>PMID:11316813</ref> <ref>PMID:18438403</ref> <ref>PMID:20118233</ref> <ref>PMID:22387026</ref>	+	[https://www.uniprot.org/uniprot/EHMT2_HUMAN EHMT2_HUMAN] Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.<ref>PMID:8457211</ref> <ref>PMID:11316813</ref> <ref>PMID:18438403</ref> <ref>PMID:20118233</ref> <ref>PMID:22387026</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Euchromatic histone-lysine N-methyltransferase 1 (EHMT1; G9a-like protein; GLP) and euchromatic histone-lysine N-methyltransferase 2 (EHMT2; G9a) are protein lysine methyltransferases that regulate gene expression and are essential for development and the ability of organisms to change and adapt. In addition to ankyrin repeats and the catalytic SET domain, the EHMT proteins contain a unique cysteine-rich region (CRR) that mediates protein-protein interactions and recruitment of the methyltransferases to specific sites in chromatin. We have determined the structure of the CRR from human EHMT2 by X-ray crystallography and show that the CRR adopts an unusual compact fold with four bound zinc atoms. The structure consists of a RING domain preceded by a smaller zinc-binding motif and an N-terminal segment. The smaller zinc-binding motif straddles the N-terminal end of the RING domain, and the N-terminal segment runs in an extended conformation along one side of the structure and interacts with both the smaller zinc-binding motif and the RING domain. The interface between the N-terminal segment and the RING domain includes one of the zinc atoms. The RING domain is partially sequestered within the CRR and unlikely to function as a ubiquitin ligase.
		+
		+	The structure of the cysteine-rich region from human histone-lysine N-methyltransferase EHMT2 (G9a).,Kerchner KM, Mou TC, Sun Y, Rusnac DV, Sprang SR, Briknarova K J Struct Biol X. 2021 Jun 25;5:100050. doi: 10.1016/j.yjsbx.2021.100050. , eCollection 2021. PMID:34278292<ref>PMID:34278292</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6mm1" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Briknarova, K]]	+	[[Category: Briknarova K]]
-	[[Category: Kerchner~~, K M~~]]	+	[[Category: Kerchner KM]]
-	[[Category: Mou~~, T C~~]]	+	[[Category: Mou TC]]
-	[[Category: Sprang~~, S R]]~~	+	[[Category: Sprang SR]]
-	~~[[Category: Cysteine-rich region]]~~	+
-	~~[[Category: Ring-like]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Zinc-binding~~]]	+

OCA at 11:25, 1 January 2020

2020-01-01T11:25:51Z

←Older revision		Revision as of 11:25, 1 January 2020
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	<StructureSection load='6mm1' size='340' side='right'caption='[[6mm1]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='6mm1' size='340' side='right'caption='[[6mm1]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6mm1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MM1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MM1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6mm1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MM1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MM1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EHMT2, BAT8, C6orf30, G9A, KMT1C, NG36 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mm1 OCA], [http://pdbe.org/6mm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mm1 RCSB], [http://www.ebi.ac.uk/pdbsum/6mm1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mm1 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mm1 OCA], [http://pdbe.org/6mm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mm1 RCSB], [http://www.ebi.ac.uk/pdbsum/6mm1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mm1 ProSAT]</span></td></tr>
	</table>		</table>
Line 13:		Line 14:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Briknarova, K]]		[[Category: Briknarova, K]]

OCA at 10:26, 2 October 2019

2019-10-02T10:26:36Z

←Older revision		Revision as of 10:26, 2 October 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6mm1 is ~~ON HOLD until Paper Publication~~	+	==Structure of the cysteine-rich region from human EHMT2==
-		+	<StructureSection load='6mm1' size='340' side='right'caption='[[6mm1]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~Authors~~: ~~Kerchner~~, K.M., ~~Mou~~, T.C., ~~Sprang, S~~.R., ~~Briknarova, K~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6mm1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MM1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MM1 FirstGlance]. <br>
-	~~Description~~: ~~Structure~~ of the ~~cysteine~~-~~rich region from human EHMT2~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mm1 OCA], [http://pdbe.org/6mm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mm1 RCSB], [http://www.ebi.ac.uk/pdbsum/6mm1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mm1 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/EHMT2_HUMAN EHMT2_HUMAN]] Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.<ref>PMID:8457211</ref> <ref>PMID:11316813</ref> <ref>PMID:18438403</ref> <ref>PMID:20118233</ref> <ref>PMID:22387026</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Briknarova, K]]		[[Category: Briknarova, K]]
-	[[Category: ~~Mou~~, ~~T.C~~]]	+	[[Category: Kerchner, K M]]
-	[[Category: ~~Kerchner~~, ~~K.M~~]]	+	[[Category: Mou, T C]]
-	[[Category: Sprang, S.R]]	+	[[Category: Sprang, S R]]
		+	[[Category: Cysteine-rich region]]
		+	[[Category: Ring-like]]
		+	[[Category: Transferase]]
		+	[[Category: Zinc-binding]]

OCA at 04:28, 24 October 2018

2018-10-24T04:28:24Z

←Older revision		Revision as of 04:28, 24 October 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6mm1 is ON HOLD	+	The entry 6mm1 is ON HOLD until Paper Publication

	Authors: Kerchner, K.M., Mou, T.C., Sprang, S.R., Briknarova, K.		Authors: Kerchner, K.M., Mou, T.C., Sprang, S.R., Briknarova, K.

OCA: Protected "6mm1" [edit=sysop:move=sysop]

2018-10-10T06:30:47Z

Protected "6mm1" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:30, 10 October 2018

OCA: New page: '''Unreleased structure''' The entry 6mm1 is ON HOLD Authors: Kerchner, K.M., Mou, T.C., Sprang, S.R., Briknarova, K. Description: Structure of the cysteine-rich region from human EHMT...

2018-10-10T06:30:46Z

New page: '''Unreleased structure''' The entry 6mm1 is ON HOLD Authors: Kerchner, K.M., Mou, T.C., Sprang, S.R., Briknarova, K. Description: Structure of the cysteine-rich region from human EHMT...

New page

'''Unreleased structure'''

The entry 6mm1 is ON HOLD

Authors: Kerchner, K.M., Mou, T.C., Sprang, S.R., Briknarova, K.

Description: Structure of the cysteine-rich region from human EHMT2
[[Category: Unreleased Structures]]
[[Category: Briknarova, K]]
[[Category: Mou, T.C]]
[[Category: Kerchner, K.M]]
[[Category: Sprang, S.R]]